ID A0A0B5D449_9CORY Unreviewed; 620 AA.
AC A0A0B5D449;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:AJE33601.1};
GN ORFNames=B842_08760 {ECO:0000313|EMBL:AJE33601.1};
OS Corynebacterium humireducens NBRC 106098 = DSM 45392.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE33601.1, ECO:0000313|Proteomes:UP000031524};
RN [1] {ECO:0000313|EMBL:AJE33601.1, ECO:0000313|Proteomes:UP000031524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFC-5 {ECO:0000313|Proteomes:UP000031524};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium humireducens DSM 45392(T),
RT isolated from a wastewater-fed microbial fuel cell.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP005286; AJE33601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5D449; -.
DR STRING; 1223515.B842_08760; -.
DR KEGG; chm:B842_08760; -.
DR HOGENOM; CLU_009289_6_5_11; -.
DR Proteomes; UP000031524; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR Gene3D; 3.30.450.330; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 49..230
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 277..596
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 471..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 66719 MW; F5BB6327396ECEEE CRC64;
MMVTRMRVIL NIFLVIALVL VGRLAWVQVV WGPDLAAKAQ EQRARVYVDP ARRGEIVDRR
GNQLAYTMQA RSLTVSPRLL RSELRQQQDL AMRIDGMSRA DIDSQIDGRV EDVLVRMSEE
IPRMIEDAGA ITGEVKSQEI LDKLHAETNY EVLVRNVDPD VATEIASTFH GVAADHQDIR
QYPNGAIAEN IIGKVSMDGQ GQFGFEASGD AMLSGINGRS TEDVSTDGQV IPGTLRDVVP
AVDGSSIELT LDLDLQTYVQ QLLEQAKANS QAKSAEAVVL DVATGKVLAM ANTDTIDPNG
NIERQLEQGK DFENQPISHP YEPGSVAKVI TAAATLEEGL TTPDEVHQVP GSIHMAGVTV
SDAWDHGLVP YTTTGIFGKS SNVGTLMLAE RLGEDRFADY LDRFGVGRPT GVELPNESAG
LLPPREQWSG GTFANLPIGQ GMSFTTLQMA SIYQALANHG ERIEPRIIES VTGPDGKVTS
TTEPRRTQVV SPQTAETVVQ MFRSVMQNDP GGLQSGTGAN GAVPGYQTAG KTGTAQKVDP
RTGAYSNSDY WITFAGIAPA DDPRFVVAVM VDEPRAGVEA GGGGGQSSAP LFRDIASWLL
NRDNIPASPP MEDMLILHAH
//
